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The membrane anchored serine protease Testisin in sperm biology
Author(s) -
Antalis Toni M,
NetzelArnett Sarah,
Hess Rex A.,
Bugge Thomas H.
Publication year - 2006
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.20.4.a49-b
Subject(s) - serine protease , sperm , serine , microbiology and biotechnology , masp1 , protease , reproductive biology , chemistry , biology , biochemistry , genetics , enzyme , embryo , embryogenesis , phosphorylation
Serine proteases are well recognized for their critical roles in proteolytic cascades associated with coagulation, fibrinolysis, complement activation, and also reproduction. Testisin (PRSS21) belongs to a unique subgroup of trypsin‐like serine proteases synthesized with a distinct carboxy‐terminal peptide that functions as a signal for membrane attachment via a glycosyl‐phosphatidyl‐inositol (GPI)‐linkage. Testisin is abundantly expressed in male germ cells and overexpressed in ovarian cancers. Testisin is an attractive target for anti‐tumor therapies, particularly for female cancers, since it is only highly expressed in the testis with relatively little expression in other normal tissues. To elucidate its function in mammalian physiology, a null mutation was introduced into the Testisin gene of mice through disruption of the Testisin coding sequence by homologous recombination. Testisin deficiency in mice resulted in compromised male fertility due to reduced fertilization of oocytes. The Testisin−/− spermatozoa are characterized by reduced motility, susceptibility to decapitation, and reduced ability to fertilize oocytes in vitro , although sperm‐oocyte binding was unaffected. The Testisin null mouse promises to be an interesting and unique model for understanding the physiological functions of Testisin in male fertility and epithelial ovarian cancer growth and progression.